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Database: UniProt
Entry: A0A1G4FIS4_9FIRM
LinkDB: A0A1G4FIS4_9FIRM
Original site: A0A1G4FIS4_9FIRM 
ID   A0A1G4FIS4_9FIRM        Unreviewed;      1099 AA.
AC   A0A1G4FIS4;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   Name=pcrA_1 {ECO:0000313|EMBL:SCL86491.1};
GN   ORFNames=PP176A_1095 {ECO:0000313|EMBL:SCL86491.1};
OS   Sporanaerobacter sp. PP17-6a.
OC   Bacteria; Bacillota; Tissierellia; Tissierellales; Sporanaerobacteraceae;
OC   Sporanaerobacter.
OX   NCBI_TaxID=1891289 {ECO:0000313|EMBL:SCL86491.1, ECO:0000313|Proteomes:UP000179042};
RN   [1] {ECO:0000313|EMBL:SCL86491.1, ECO:0000313|Proteomes:UP000179042}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PP176A {ECO:0000313|EMBL:SCL86491.1};
RA   Seilhamer J.J.;
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=5.6.2.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00034618};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by
CC         translocating in the 3'-5' direction.; EC=5.6.2.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00034617};
CC   -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC       {ECO:0000256|ARBA:ARBA00009922}.
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DR   EMBL; FMIF01000010; SCL86491.1; -; Genomic_DNA.
DR   RefSeq; WP_071139431.1; NZ_FMIF01000010.1.
DR   AlphaFoldDB; A0A1G4FIS4; -.
DR   Proteomes; UP000179042; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   CDD; cd17932; DEXQc_UvrD; 1.
DR   CDD; cd19067; PfuEndoQ-like; 1.
DR   CDD; cd18807; SF1_C_UvrD; 1.
DR   Gene3D; 1.10.10.160; -; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
DR   InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR   InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR016195; Pol/histidinol_Pase-like.
DR   InterPro; IPR014016; UvrD-like_ATP-bd.
DR   PANTHER; PTHR11070:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 1.
DR   PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR   Pfam; PF00580; UvrD-helicase; 1.
DR   Pfam; PF13361; UvrD_C; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF89550; PHP domain-like; 1.
DR   PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR   PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Helicase {ECO:0000256|PROSITE-ProRule:PRU00560,
KW   ECO:0000313|EMBL:SCL86491.1};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00560,
KW   ECO:0000313|EMBL:SCL86491.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000179042}.
FT   DOMAIN          469..731
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          732..1011
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   REGION          425..469
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        428..449
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         490..497
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   1099 AA;  124953 MW;  B6C637EA6AA22893 CRC64;
     MFIADFHIHS KYSRATSKEC IPEILEMWSR RKGINLLGTA DFTHPVWREE LKEKLTPSEE
     GLYVLKDDYR KEDNIGGTDF KPRFIISGEI SSIYKKNGKV RKIHNLILLP GLEEAELISH
     RLEAIGNLHS DGRPILGLDS KDLLEIVLDI CPEAIFIPAH IWTPHFSLYG EYSGFDDIRE
     CFKDLTDNIY AVETGLSSDP PMNWRLSALD KFTLVSNSDA HSPANLAREA NIFDTDLSYS
     NISQALKNRN TKEFYGTIEF FPEEGKYHYD GHRNCKVCLK PAETEALSGI CPVCGGRLTV
     GVLHRVEALA DRAEGFVPQT AKHFESLVPL REIIASSLGF TTASIKVKRR YENLIQTLGT
     ELFILREASL SDIELAAGPH IAEGIRRLRA GQVEIHPGYD GKYGQINVMN KNEINLISGQ
     ISLFKNEDNN DRNNDKNNDI QKQSLIKKER VSEPYSASSI EPLPSSNPYR LNQEQWEDVS
     SPEPVIVVMA GPGTGKTRTL VYRIVYLIEN CGISPSEITA VTFTNKAANE MRSRLEKHFK
     NKNTVKAMNI GTFHSICLKI LSEEKGNGKT TIIDEYNSIS IVEDILKNLQ LKISPRDAMK
     EISLMKSGTI SGEENKKELK IPLEVYDLYC SQLKQYDVMD YDDILLEALK KFKNTNLSNS
     FSYLLVDEFQ DINEIQYRLI KEWASNNIFV IGDPEQSIYG FRGSDFRYFD IFKENFPHAK
     NIRLIQNYRS TPEIIHCAKS VISKKIKGEP FSFLESKREK GTKVRLLKTN NEFSEALFVA
     KEINRIVGGI DMIDTQKISE TDRKNSKVKN PRSFADIAIL YRTNHQANII EQCLIKEGIP
     YVVAGKDEFL SEKEVRAVIA FFQFLLNPKD IFSLKTYLKI SGIYSTELIQ EILKNYVSAK
     KNIPSLIKII EKVQPSDDLV KSWNFIELLK KYEPLLHKEK PVKLIDSWIN DNNLSGIDCL
     KLLLNTSVFH NNMPSFIQTL ILGHESDVVR SSSKIYSSDA VSLMTIHGSK GLEFPVIFIC
     GVNDGLIPLK NSGRDFNLDE ERRLFYVGMT RAQDELILIT SHDRPSPFIS DIPEDSIIKE
     NTSTNKHRPQ SKQLSIFDI
//
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